Summary:
The purified and reconstituted PreA/PreT complex was shown to have NAD-dependent dihydropyrimidine dehydrogenase activity [Mihara08, Hidese11]. The enzyme appears to produce dihydrouracil during exponential growth and during stationary phase convert it back to uracil, which can be incorporated into nucleic acids [Hidese11].

A preTA-deficient mutant has no growth defect in LB medium, but it is not producing dihydrouracil [Hidese11].

Summary:
Based on sequence similarity, PreT was predicted to be a dihydrothymine dehydrogenase or glutamate synthase [Reed03, Serres01]. PreT has similarity to the N-terminal half of mammalian dihydropyrimidine dehydrogenase [Hidese11].

Summary:
Based on sequence similarity, PreA was predicted to be a dihydrothymine/dihydropyrimidine dehydrogenase [Reed03, Serres01]. PreA has similarity to the C-terminal half of mammalian dihydropyrimidine dehydrogenase [Hidese11].